The reduction of Mo-thiocyanate (V) complex on dropping mercury electrode has been studied at ionic strength 0.6 with pH less than 2.3. D-C polarogram obtained from acidic solutions are reversible, diffusion controlled current. The electrode reaction of Mo-thiocyanate(V) may be represented as follows. $MoO(SCN)_3\;+\;2H^+\;+\;2e\;{\to}\;Mo(SCN)_2{^+}\;+\;H_2O\;+\;SCN^-$From this reaction, the half wave potential assumed to be Considering the dissociation of this complex, however, it was estimated that the electrode reaction may be written by.

Band assignments in the infrared absorption spectra of the four substituted Urea compounds, Fenuron (3-phenyl-1,1-dimethyl urea), OMU (3-cyclooctyl-1,1-dimethyl urea), Herban (3-(hexahydro-4,7-methanoidan-5-yl)-l,1-dimethyl urea), and Monuron (3-(p-chlorophenyl)-1,1-dimethyl urea), are made by analyzing the spectra obtained with various solvents. The results suggest that Fenuron and Monuron, each of which contain an unsaturated benzene ring, have a strong tendency to bond through both the amino group and the carbonyl oxygen. Herban and OMU, however, exhibit a much greater change in strength of the carbonyl bond than of the amino bond. It means that a strong hydrogen bonding occurs only at the carbonyl oxygen in the compounds.

The kinetics of the pepsin-catalyzed hydrolysis of N-carbobenzoxy-L-glutamyl-L-tyrosine at pH 3.5 and were determined by a spectrophotometric technique. The pepsin used was further purified on a Sephadex G-75 column. The kinetics data were Km = l.7 = 3.99Kcal/mole, and . An analysis of the above data and other investigators' data obtained from some dipeptides led to the following conclusions. (1) Phenylalanyl residues in a synthetic peptide are bound to pepsin more strongly than glutamyl or tyrosyl residues, supporting the theory that a part of the binding region of the active center is hydrophobic. (2) Dipeptides are bound to pepsin principally through their side chains and the binding involves both side-chain residues. (3) The nature of amino acids in dipeptides values.

In order to obtain the more effective evidence, supporting the hypothesis which have been previously described by former report that pepsin (EC 3.4. 4.1) forms a hydrophobic bond with the nonpolar side chain of its substrate, the inhibitory effect of carboxylic acids(from formic acid to iso-butyric acid) on the activity of pepsin to the synthetic dipeptide, N-Carbobenzoxy-L-glutamyl-L-tyrosine, was discussed. The kinetic study showed that the inhibition by carboxylic acids was competitive. The Kidecreased with increasing size of the inhibitor molecule. The increased linearly with increasing number of carbon atoms in the hydrocarbon chain of the inhibitor. It was confirmed that the hydrophobic bond between more than one side chain of amino acid residues(phenylalanine) in the binding region of the active center of pepsin and the side chain of amino acid residues in the substrate was formed as the first step of its enzymic mechanism. The inhibitory effect of carboxylic acids was due to the competition of the hydrocarbon group of the carboxylic acids with the side chain of the substrate for the hydrophobic binding site(the side chain of phenylalanine) of the pepsin.

A study was made on the radioiodination of organic compounds in presence of hydrogen peroxide both in aqueous and organic solvent systems. In case of the reaction of rosebengal, Hippuran, and 5-iodo-uracil the aqueous reaction system could give high labelling yield within a relatively short reaction time. Labelling yield of average 50% could be obtained within 30 minutes of reaction sequence. In cases of organic solvent systems (D.M.S.O., D.M.F., and Dioxane) the solvent system of D.M.S.O. could give better yield for neutral organic compounds, where as D.M.F. and Dioxane gave better labelling result for acidic materials. Especially, o-iodobenzoic acid, o-iodotoluene, and pentachlorophenol could be labelled better in organic solvent system.

Four-ball EP and wear testers were used to study the effects of thickeners and additives on the EP and wear properties of some Korean greases. The EP property improved in the order of Li < Al < Ca, and the concentration of thickener did not affect the property when the same base oil and additives were used. The anti-wear property was improved in general when the additives were used.

The extension of the theory of the electrolyte solution to the calculation of the hydration number and the mean activity coefficient of some 1:1 electrolytes in the concentrated solutions has been made. In this derivation, the hydration number has been calculated from the equation of the dielectric constant proposed by Hobbs, Jhon, and Eyring, and the mean activity coefficient from the theoretical formula developed by Jhon and Eyring. The agreement between theory and experiment over a.wide concentration range is quite satisfactory.

Further validity of the significant structure theory has been tested by calculating the viscosities of binary mixtures-three pairs of -and also by calculating the viscosities of n- in the pressure range of 1 bar to 4000 bars. The results are quite satisfactory for both cases and provide another evidence for the validity of the significan structure theory.